Our research goals for the coming year include: (1) thorough kinetic studies of beta-aminoethyl phosphate triesters extended to diesters as well as to the effect of metal ions in order to establish the requisite Bronsted relationships; (2) to determine the effect of active site modification on the mechanism of FBPase action in order to implicate the specific role of the enzymic ligands in the catalysis; (3) the extension of binding studies involving substrate analogs and products to monitor the effect of an allosteric modifier, adenosine monophosphate, on these parameters, thereby gaining initial indications as to how the modifier may inhibit this enzyme; (4) the initiation of stereochemical studies involving chiral phosphorothioate substrates and acid phosphatases in order to define the stereochemical events involved in the phosphoryl transfer catalyzed by these enzymes.